Structure of PDB 5ex6 Chain C

Receptor sequence
>5ex6C (length=388) Species: 55952 (Streptomyces toyocaensis) [Search protein sequence]
RPPIHTLRQGFDPADELRAAGELTRVRLGAEHTWLATGHDVVRQVLGDHT
RFSTRRRFDRDEIGGKGVFRPRELVGNLMDYDPPEHTRLRRLLAPGFTHR
KIRRMAPYIEQIVTERLDEMEREGSPADLIELFADEVPGPVLCELLGVPR
DDRAMFLQLCHRHLDASLSGRRRAAAGEAFSRYLVTMVARERKDPGDGLI
GMVVAEHGDTVTDEELRGVCVQMMLAGDDNISGMIGLGVLALLRNPEQIA
ALRGDVPAAERAVDELIRYLTVPYAPTPRTAIEDSTVGDQVIKAGETVLC
SLPTANRDPALLPDADRLDVTREAVPHVAFGHGVHHCLGAALARLELRIA
YTALWRRFPDLRLADPDGATEFRLSTPAYGISRLMVTW
3D structure
PDB5ex6 More than just recruitment: the X-domain influences catalysis of the first phenolic coupling reaction in A47934 biosynthesis by Cytochrome P450 StaH.
ChainC
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D175 A236 D239 N240 I241 C347 L348 G349 E356 A388
Catalytic site (residue number reindexed from 1) D165 A226 D229 N230 I231 C337 L338 G339 E346 A378
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM C L88 M89 H96 R100 M233 A236 G237 N240 P283 P286 T287 R289 A339 F340 H345 C347 A353 L78 M79 H86 R90 M223 A226 G227 N230 P273 P276 T277 R279 A329 F330 H335 C337 A343
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:5ex6, PDBe:5ex6, PDBj:5ex6
PDBsum5ex6
PubMed27477788
UniProtQ8KLL9

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